Liang Tong Lab at Columbia University

The Pyruvate Carboxylase (PC) Project

Updated Jan. 2018

Pyruvate carboxylase (PC) catalyzes the biotin-dependent carboxylation of pyruvate to produce oxaloacetate. PC has crucial roles in gluconeogenesis, lipogenesis, glyceroneogenesis, and insulin secretion in mammals. PC deficiencies are linked to lactic acidemia, hypoglycemia, and other diseases. Four single-site mutations, V145A, R451C, A610T, M743I, are associated with these diseases.

PC is a multi-domain enzyme of about 130 kD in eukaryotes and most bacteria. It contains the biotin carboxylase (BC), carboxyltransferase (CT), and biotin-carboxyl carrier protein (BCCP) domains. The BC domain catalyzes the first step of the reaction: the carboxylation of the biotin prosthetic group that is covalently linked to BCCP. In the second step of the reaction, the carboxyltransferase (CT) domain catalyzes the transfer of the carboxyl group from (carboxy)biotin to pyruvate.

PC is only active in the tetrameric form. The catalytic activity is stimulated by acetyl-CoA and inhibited by aspartate.

Major findings from this project

Publications from this project

Funding for this project


© copyright 2008-2018, Liang Tong.